메뉴 건너뛰기




Volumn 102, Issue 6, 2009, Pages 1570-1581

Mechanism of cellulase reaction on pure cellulosic substrates

Author keywords

Cello oligosaccharides; Cellulase; Crystallinity; DP; NCC

Indexed keywords

CELLO-OLIGOSACCHARIDES; CELLULASE; CRYSTALLINITY; DP; NCC;

EID: 65349184491     PISSN: 00063592     EISSN: 10970290     Source Type: Journal    
DOI: 10.1002/bit.22195     Document Type: Article
Times cited : (97)

References (31)
  • 2
    • 11144305875 scopus 로고    scopus 로고
    • Study on crystal structures of enzyme-hydrolyzed cellulosic materials by X-ray diffraction
    • Cao Y, Tan H. 2005. Study on crystal structures of enzyme-hydrolyzed cellulosic materials by X-ray diffraction. Enzyme Microb Technol 36: 314-317.
    • (2005) Enzyme Microb Technol , vol.36 , pp. 314-317
    • Cao, Y.1    Tan, H.2
  • 3
    • 0024031733 scopus 로고
    • A model of enzyme adsorption and hydrolysis of microcrystalline cellulose with slow deactivation of the adsorbed enzyme
    • Converse AO, Matsuno R, Tanaka M, Taniguchi M. 1988. A model of enzyme adsorption and hydrolysis of microcrystalline cellulose with slow deactivation of the adsorbed enzyme. Biotechnol Bioeng 32: 38-45.
    • (1988) Biotechnol Bioeng , vol.32 , pp. 38-45
    • Converse, A.O.1    Matsuno, R.2    Tanaka, M.3    Taniguchi, M.4
  • 4
    • 0345676498 scopus 로고    scopus 로고
    • High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei
    • Divne C, Stahlberg J, Teeri TT, Jones TA. 1998. High-resolution crystal structures reveal how a cellulose chain is bound in the 50 A long tunnel of cellobiohydrolase I from Trichoderma reesei. J Mol Biol 275:309-325.
    • (1998) J Mol Biol , vol.275 , pp. 309-325
    • Divne, C.1    Stahlberg, J.2    Teeri, T.T.3    Jones, T.A.4
  • 5
    • 0036233797 scopus 로고    scopus 로고
    • A model explaining declining rate in hydrolysis oflignocellulosic substrates with cellobiohydrolase I (Cel7A) and endoglucanase (Cel7B) of Trichoderma reesei
    • Eriksson T, Karlson J, Tjerneld F. 2002. A model explaining declining rate in hydrolysis oflignocellulosic substrates with cellobiohydrolase I (Cel7A) and endoglucanase (Cel7B) of Trichoderma reesei. Appl Biochem Biotechnol 101:41-60.
    • (2002) Appl Biochem Biotechnol , vol.101 , pp. 41-60
    • Eriksson, T.1    Karlson, J.2    Tjerneld, F.3
  • 7
    • 65349169112 scopus 로고
    • Recovery and reutilization of cellulases used for the hydrolysis of woods. V. Adsorption mechanism of β-glucosidase on cellulosic materials
    • Fujishima S, Yaku F, Koshijima T. 1989. Recovery and reutilization of cellulases used for the hydrolysis of woods. V. Adsorption mechanism of β-glucosidase on cellulosic materials. Mokuzai Gakkaishi 35(9):845-850.
    • (1989) Mokuzai Gakkaishi , vol.35 , Issue.9 , pp. 845-850
    • Fujishima, S.1    Yaku, F.2    Koshijima, T.3
  • 8
    • 0038019825 scopus 로고    scopus 로고
    • Kinetic dynamics in heterogeneous enzymatic hydrolysis of cellulose: An overview, an experimental study and mathematical modeling
    • Gan Q, Allen SJ, Taylor G. 2003. Kinetic dynamics in heterogeneous enzymatic hydrolysis of cellulose: An overview, an experimental study and mathematical modeling. Proc Biochem 38:1003-1018.
    • (2003) Proc Biochem , vol.38 , pp. 1003-1018
    • Gan, Q.1    Allen, S.J.2    Taylor, G.3
  • 16
  • 17
    • 0027498223 scopus 로고
    • The use of enzyme recycling and the influence of sugar accumulation on cellulose hydrolysis by Tricho-derma cellulases
    • Ramos LP, Breuil C, Saddler JN. 1993. The use of enzyme recycling and the influence of sugar accumulation on cellulose hydrolysis by Tricho-derma cellulases. Enzyme Microb Technol 15:19-25.
    • (1993) Enzyme Microb Technol , vol.15 , pp. 19-25
    • Ramos, L.P.1    Breuil, C.2    Saddler, J.N.3
  • 18
    • 0037790301 scopus 로고
    • Degradation of polymeric carbohydrates by microbial enzymes
    • Resse ET. 1977. Degradation of polymeric carbohydrates by microbial enzymes. Recent Adv Phytochem 7:311-367.
    • (1977) Recent Adv Phytochem , vol.7 , pp. 311-367
    • Resse, E.T.1
  • 19
    • 0033949359 scopus 로고    scopus 로고
    • A note on the estimation of microbial glycosidase activities by dinitrosalicylic acid reagent
    • Sengupta S, Jana ML, Sengupta D, Naskar AK. 2000. A note on the estimation of microbial glycosidase activities by dinitrosalicylic acid reagent. Appl Microb Biotechnol 53:732-735.
    • (2000) Appl Microb Biotechnol , vol.53 , pp. 732-735
    • Sengupta, S.1    Jana, M.L.2    Sengupta, D.3    Naskar, A.K.4
  • 20
    • 0043093279 scopus 로고    scopus 로고
    • Analysis of molecular size distributions of cellulose molecules during hydrolysis of cellulose by recombinant Cellulomonas fimih-1,4-glucanases
    • Stalbrand H, Mansfield SD, Saddler JN, Kilburn DG, Warren RAJ, Gilkes NR. 1998. Analysis of molecular size distributions of cellulose molecules during hydrolysis of cellulose by recombinant Cellulomonas fimih-1,4-glucanases. Appl Environ Microbiol 64:2374-2379.
    • (1998) Appl Environ Microbiol , vol.64 , pp. 2374-2379
    • Stalbrand, H.1    Mansfield, S.D.2    Saddler, J.N.3    Kilburn, D.G.4    Warren, R.A.J.5    Gilkes, N.R.6
  • 21
    • 65349164395 scopus 로고
    • Molecular properties of cellulose
    • New York: The Ronald Press company, pp
    • Stamm AJ. 1964. Molecular properties of cellulose. In: Wood and cellulose science. New York: The Ronald Press company, pp. 78-121.
    • (1964) Wood and cellulose science , pp. 78-121
    • Stamm, A.J.1
  • 22
    • 0034204550 scopus 로고    scopus 로고
    • Trichoderma reesei cellulases and their core domain in the hydrolysis and modification of chemical pulp
    • Suurnakki A, Tenkanen M, Sika-aho M, Niku-paavola ML, Viikari L, Buchert J. 2000. Trichoderma reesei cellulases and their core domain in the hydrolysis and modification of chemical pulp. Cellulose 7:189-209.
    • (2000) Cellulose , vol.7 , pp. 189-209
    • Suurnakki, A.1    Tenkanen, M.2    Sika-aho, M.3    Niku-paavola, M.L.4    Viikari, L.5    Buchert, J.6
  • 23
    • 0033485705 scopus 로고    scopus 로고
    • Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I
    • Valjamae P, Sild V, Nutt A, Pettersson G, Johansson G. 1999. Acid hydrolysis of bacterial cellulose reveals different modes of synergistic action between cellobiohydrolase I and endoglucanase I. Eur J Biochem 266(2):327-334.
    • (1999) Eur J Biochem , vol.266 , Issue.2 , pp. 327-334
    • Valjamae, P.1    Sild, V.2    Nutt, A.3    Pettersson, G.4    Johansson, G.5
  • 24
    • 0032522362 scopus 로고    scopus 로고
    • The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model
    • Valjamae P, Sild V, Pettersson G, Johansson G. 1998. The initial kinetics of hydrolysis by cellobiohydrolases I and II is consistent with a cellulose surface-erosion model. Eur J Biochem 253(2):469-475.
    • (1998) Eur J Biochem , vol.253 , Issue.2 , pp. 469-475
    • Valjamae, P.1    Sild, V.2    Pettersson, G.3    Johansson, G.4
  • 25
    • 0025881547 scopus 로고
    • Enzymatic hydrolysis of cellulose: An overview
    • Walker LP, Wilson DB. 1991. Enzymatic hydrolysis of cellulose: An overview. Bioresour Technol 36:3-14.
    • (1991) Bioresour Technol , vol.36 , pp. 3-14
    • Walker, L.P.1    Wilson, D.B.2
  • 26
    • 32544437997 scopus 로고    scopus 로고
    • Changes in the structural properties and rate of hydrolysis of cotton fibers during extended enzymatic hydrolysis
    • Wang L, Zhang Y, Gao P, Shi D Liu H, Gao H. 2005. Changes in the structural properties and rate of hydrolysis of cotton fibers during extended enzymatic hydrolysis. Biotechnol Bioeng 93(3):443-456.
    • (2005) Biotechnol Bioeng , vol.93 , Issue.3 , pp. 443-456
    • Wang, L.1    Zhang, Y.2    Gao, P.3    Shi, D.4    Liu, H.5    Gao, H.6
  • 27
    • 0016685689 scopus 로고
    • Properties and mode of action of cellulases
    • Wood TM. 1975. Properties and mode of action of cellulases. Biotechnol Bioeng 5:111-137.
    • (1975) Biotechnol Bioeng , vol.5 , pp. 111-137
    • Wood, T.M.1
  • 28
    • 33747114376 scopus 로고    scopus 로고
    • Change in the enzymatic hydrolysis rate ofavicel cellulose with conversion
    • Yang B, Willies DM, Wyman CE. 2006. Change in the enzymatic hydrolysis rate ofavicel cellulose with conversion. Biotechnol Bioeng 94(6):1122-1128.
    • (2006) Biotechnol Bioeng , vol.94 , Issue.6 , pp. 1122-1128
    • Yang, B.1    Willies, D.M.2    Wyman, C.E.3
  • 29
    • 20344363170 scopus 로고    scopus 로고
    • Determination of the number-average degree of polymerization of cellodextrins and cellulose with application to enzymatic hydrolysis
    • Zhang YHP, Lynd LR. 2005. Determination of the number-average degree of polymerization of cellodextrins and cellulose with application to enzymatic hydrolysis. Biomacromolecules 6:1510-1515.
    • (2005) Biomacromolecules , vol.6 , pp. 1510-1515
    • Zhang, Y.H.P.1    Lynd, L.R.2
  • 30
    • 33746879626 scopus 로고    scopus 로고
    • A functionally based model for hydrolysis of cellulose by fungal cellulase
    • Zhang YHP, Lynd LR. 2006. A functionally based model for hydrolysis of cellulose by fungal cellulase. Biotechnol Bioeng 94:889-898.
    • (2006) Biotechnol Bioeng , vol.94 , pp. 889-898
    • Zhang, Y.H.P.1    Lynd, L.R.2
  • 31
    • 10844286172 scopus 로고    scopus 로고
    • Towards an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems
    • Zhang YHP, Lynd LR. 2004. Towards an aggregated understanding of enzymatic hydrolysis of cellulose: Noncomplexed cellulase systems. Biotechnol Bioeng 88:797-824.
    • (2004) Biotechnol Bioeng , vol.88 , pp. 797-824
    • Zhang, Y.H.P.1    Lynd, L.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.